Transglycosylation activity of cellobiohydrolase I from Trichoderma longibrachiatum on synthetic and natural substrates

Using 4-methylumbelliferyl (MUF) ß- d-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In...

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Published inBiochimica et biophysica acta Vol. 1073; no. 3; pp. 481 - 485
Main Authors Gusakov, Alexander V., Protas, Oksana V., Chernoglazov, Vladimir M., Sinitsyn, Arkady P., Kovalysheva, Galina V., Shpanchenko, Olga V., Ermolova, Olga V.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 09.04.1991
Elsevier
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Summary:Using 4-methylumbelliferyl (MUF) ß- d-cellobioside as a substrate, the ability of cellobiohydrolase I from Trichoderma longibrachiatum to catalyze transglycosylation has been demonstrated. At substrate concentrations greater than 2 mM, the formation of MUF-tetrasaccharide was detected using HPLC. In the course of enzymatic reaction, a concentration of the transglycosylation product passed through a maximum, since at later stages of the reaction the product was further hydrolyzed. At MUF-ß- d-cellobioside concentrations of 2–10 mM, the maximum weight content of MUF-tetrasaccharide amounted to 1–4% of the total content of saccharides. In the reaction system, containing 2.5 mM MUF-ß- d-cellobioside and 10 mM MUF-ß- d-glucoside MUF-trisaccharide was formed as the main transglycosylation product. In hydrolysis of natural substrates (cellulose and cellotriose) in the presence of MUF-ß- d-glucoside a formation of MUF-trisaccharide was also observed.
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ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(91)90219-7